WO2005076013B1 - Process for screening glycoform-specific antibodies - Google Patents
Process for screening glycoform-specific antibodiesInfo
- Publication number
- WO2005076013B1 WO2005076013B1 PCT/EP2005/001160 EP2005001160W WO2005076013B1 WO 2005076013 B1 WO2005076013 B1 WO 2005076013B1 EP 2005001160 W EP2005001160 W EP 2005001160W WO 2005076013 B1 WO2005076013 B1 WO 2005076013B1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- glycoprotein
- glycoform
- essentially
- recombinant human
- less
- Prior art date
Links
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/26—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against hormones ; against hormone releasing or inhibiting factors
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6854—Immunoglobulins
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- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Immunology (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- Urology & Nephrology (AREA)
- General Health & Medical Sciences (AREA)
- Hematology (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Organic Chemistry (AREA)
- Biophysics (AREA)
- Biotechnology (AREA)
- Cell Biology (AREA)
- Genetics & Genomics (AREA)
- Microbiology (AREA)
- Endocrinology (AREA)
- Food Science & Technology (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
The present invention relates to the use of the assessment of the binding between - antibodies elicited against a first glycoprotein, and - at least one glycoform of a second glycoprotein, said second glycoprotein being itself a glycoform of the first protein, wherein said glycoform of the second glycoprotein is selected from a group of glycoforms of the second glycoprotein, each glycoform of said group corresponding to a determined glycosylation state defined by a determined sialylation state, and/or a determined branching state, and/or a determined fucosylation state, provided that said glycosylation state is not uniquely defined by a substantially unsialylated state, for the screening of glycoform specific antibodies directed against a given glycoform of the second glycoprotein.
Claims
1. The use of the assessment of the binding between
- antibodies elicited against a first glycoprotein, and
- at least one glycoform of a second glycoprotein, said second glycoprotein being itself a glycoform of the first glycoprotein, wherein said glycoform of the second glycoprotein is selected from a group of glycoforms of the second glycoprotein, each glycoform of said group corresponding to a determined glycosylation state defined by a determined branching state and a determined fucosylation and / or sialylation state, for the screening of glycoform specific antibodies directed against a given glycoform of the second glycoprotein.
2. A process for screening glycoform specific antibodies among antibodies elicited against a first glycoprotein, comprising a step of determination of the binding between
- antibodies elicited against a first glycoprotein, and
- at least one glycoform of a second glycoprotein, said second glycoprotein being itself a glycoform of the first protein, wherein said glycoform of the second glycoprotein is selected from a group of glycoforms of the second glycoprotein, each glycoform of said group corresponding to a determined glycosylation state defined by a determined branching state and a determined fucosylation and / or sialylation state, to recover antibodies liable to bind to at least one given glycoform of the second glycoprotein.
3. A process according to claim 2, wherein the glycosylation state of the glycoform of the second glycoprotein presents at least one of the following criteria:
- it is essentially more sialylated than said second glycoprotein, or
- it is essentially less sialylated than said second glycoprotein, or
- it is essentially more branched than said second glycoprotein, or
- it is essentially less branched than said second glycoprotein, or
- it is essentially more fucosylated than said second glycoprotein, or
- it is essentially less fucosylated than said second glycoprotein.
4. A process according to claim 2 or 3, wherein the binding between at least one of the antibodies elicited against the first glycoprotein and each of the glycoforms of the second glycoprotein which are respectively:
- essentially more sialylated than said second glycoprotein,
- essentially less sialylated than said second glycoprotein,
- essentially more branched than said second glycoprotein,
- essentially less branched than said second glycoprotein,
- essentially more fucosylated than said second glycoprotein, and
- essentially less fucosylated than said second glycoprotein, is determined.
5. A process according to claim 2 or 3, wherein the glycosylation state of the glycoform of the second glycoprotein presents at least two of the following criteria:
- it is essentially more sialylated or less sialylated than said second glycoprotein,
- it is essentially more branched or less branched than said second glycoprotein,
- it is essentially more fucosylated or less fucosylated than said second glycoprotein.
6. A process according to claim 5, wherein the glycosylation state of the glycoform of the second glycoprotein presents one of the following criteria:
- it is essentially more sialylated and more fucosylated than said second glycoprotein, or
- it is essentially more sialylated and less fucosylated than said second glycoprotein, or
- it is essentially more sialylated and more branched than said second glycoprotein, or
- it is essentially more sialylated and less branched than said second glycoprotein, or
- it is essentially less sialylated and more fucosylated than said second glycoprotein, or
- it is essentially less sialylated and less fucosylated than said second glycoprotein, or
- it is essentially less sialylated and more branched than said second glycoprotein, or
- it is essentially less sialylated and less branched than said second glycoprotein, or
- it is essentially more branched and more fucosylated than said second glycoprotein, or
- it is essentially more branched and less fucosylated than said second glycoprotein, or
- it is essentially less branched and more fucosylated than said second glycoprotein, or
- it is essentially less branched and less fucosylated than said second glycoprotein.
7. A process according to claim 2, 3 or 5, wherein the glycosylation state of the glycoform of the second glycoprotein presents three of the following criteria: - it is essentially more sialylated or less sialylated than said second glycoprotein,
- it is essentially more branched or less branched than said second glycoprotein,
- it is essentially more fucosylated or less fucosylated than said second glycoprotein.
8. A process according to claim 7, wherein the glycosylation state of the glycoform of the second glycoprotein presents one of the following criteria:
- it is essentially more sialylated, more branched and more fucosylated than said second glycoprotein,
- it is essentially more sialylated, more branched and less fucosylated than said second glycoprotein,
- it is essentially more sialylated, less branched and more fucosylated than said second glycoprotein,
- it is essentially more sialylated, less branched and less fucosylated than said second glycoprotein,
- it is essentially less sialylated, more branched and more fucosylated than said second glycoprotein,
- it is essentially less sialylated, more branched and less fucosylated than said second glycoprotein,
- it is essentially less sialylated, less branched and more fucosylated than said second glycoprotein,
- it is essentially less sialylated, less branched and less fucosylated than said second glycoprotein.
9. A process according to any of claims 2 to 8, wherein the antibodies elicited against the first glycoprotein bind to the second glycoprotein with an affinity equal to or higher than the binding affinity of said antibodies to the first glycoprotein.
10. A process according to any of claims 2 to 9, wherein a glycoform of the second glycoprotein of a determined glycosylation state is obtained by a combination of at least one enzymatic modification of the second glycoprotein and/or of at least one lectin fractionation.
11. A process according to claim 10, wherein the lectin is selected from the group comprising mannose-specific lectins, such as the ConA or Lentil lectins, fucose-specific lectins, such as the Ulex lectin, gactose-specific lectins, such as ricin, or sialic acid-specific lectins, such as the limulin or Sambucus nigra lectin.
12. A process according to claims 10 or 11, wherein the enzymatic modification is carried out by an enzyme selected from the group comprising a neuraminidase or a fucosidase, or a glycosyltransferase, in particular a sialyl transferase or a fucosyl transferase.
13. A process according to any of claims 10 to 12, wherein a less sialylated glycoform of the second glycoprotein as compared to the second glycoprotein is obtained by neuraminidase treatment of said second glycoprotein.
14. A process according to any of claims 10 to 13, wherein a less fucosylated glycoform of the second glycoprotein as compared to the second glycoprotein is obtained by lentil fractionation of the second glycoprotein by collecting the fraction which does not bind to lentil and a more fucosylated glycoform of the second glycoprotein as compared to the second glycoprotein is obtained by collecting the fraction which binds to lentil.
15. A process according to any of claims 10 to 14, wherein a ConA fractionation of the second glycoprotein is performed by collecting three fractions, A, B, and C, the binding of which to ConA is such that,
- C binds to ConA more strongly than B does, and
- B binds to ConA more strongly than A does, the branching state of a given fraction being essentially different from the branching state of the other two fractions.
16. A process according to any of claims 2 to 15, wherein a more sialylated glycoform of the second glycoprotein as compared to the second glycoprotein is obtained by sialytransferase treatment of said second glycoprotein or by neuraminidase treatment followed by sialyltransferase treatment of said second glycoprotein.
17. A process according to claim 12 or 16, wherein the sialyltransferase is a human α-2,6 sialyltransferase, in particular a STβGall sialyltransferase, more particularly a N-terminal shortened ST6GalI sialyltransferase deleted of at most its first 99 residues, such as represented by SEQ ID NO: 1.
18. A process according to any of claims 2 to 17, wherein, in a preliminary step, the antibodies to be screened are classified in pools, each pool being characterized in that two antibodies selected from a same pool can not bind to the same glycoprotein at the same time.
19. A process according to any of claims 2 to 18, wherein in a first step, said first step preceding the preliminary step of claim 18, it is checked that the antibodies elicited against the first glycoprotein bind to the second glycoprotein.
20. A process according to any of claims 2 to 19, wherein the binding of the antibodies to the first glycoprotein, to the second glycoprotein and to the glycoforms of the second glycoproteins is determined by using immunoassays, in particular immunoassay formats using an amplification system for detection, such as an ELISA.
21. A process according to claim 20, wherein the immunoassay is a sandwich immunoassay, in particular a sandwich ELISA test, comprising the following steps:
- fixing a capture antibody, selected from a pool such as defined in claim 18, onto a support,
- contacting a glycoprotein, corresponding to the first glycoprotein, to the second glycoprotein or to the glycoforms of the second glycoprotein, to said capture antibody, to form, if adequate, a capture antibody-glycoprotein binary complex,
- contacting a tracer antibody, selected from a pool such as defined in claim 18, provided said pool is different from the one used for the selection of said capture antibody, to said capture antibody-glycoprotein binary complex, to form, if adequate, a capture antibody-glycoprotein- tracer antibody ternary complex,
- detecting the tracer antibody for measuring the number of ternary complexes.
22. A process according to any of claims 2 to 21, wherein the first glycoprotein and the second glycoprotein are similar.
23. A process according to any of claims 2 to 21, wherein the first glycoprotein and the second glycoprotein originate from different natural tissues and/or fluids.
24. A process according to any of claims 2 to 21, wherein the first glycoprotein originates from a natural tissue and the second glycoprotein is a recombinant protein.
25. A process according to any of claims 2 to 24, wherein the first glycoprotein is a N-linked glycoprotein, such as TSH, in particular pituitary TSH, LH, FSH, or placental hCG.
26. A process according to any claim 24 or 25, wherein the first glycoprotein is pituitary or blood human TSH and the second glycoprotein is a recombinant human TSH, in particular a recombinant human TSH produced by mammalian cells.
27. The use of a glycosylation-specific antibody as screened by the process according to any of claims 2 to 26, said process comprising a step of determination of the binding between
- antibodies elicited against a first glycoprotein, and
- at least one glycoform of a second glycoprotein, said second glycoprotein being itself a glycoform of the first glycoprotein, wherein said glycoform of the second glycoprotein is selected from a group of glycoforms of the second glycoprotein, each glycoform of said group corresponding to a determined glycosylation state defined by a determined branching state and a determined fucosylation and / or sialylation state, for the binding or the purification of given glycoforms of the second glycoprotein.
28. A process for the preparation of a glycoform of a recombinant human TSH produced by mammalian cells, characterized in that said recombinant human TSH is sialylated by a human α-2,6 sialyltransferase, in particular a human SToGaII sialyltransferase, more particularly a N-terminal shortened human SToGaII sialyltransferase deleted of at most its first 99 residues, such as represented by SEQ ID NO: 1, to yield an oversialylated glycoform of the recombinant TSH bearing oΩ.,3 and cQ.,6 sialyl moieties
29. A process according to claim 28, wherein the recombinant human TSH is first treated by a neuraminidase, in particular a Clostridium perfringens or a Vibrio cholerae neuraminidase, to give a substantially unsialylated TSH, and then submitted to sialylation, to yield a resialylated glycoform of the recombinant TSH bearing essentially only o2,6 sialyl moieties.
30. A process for the preparation of a glycoform of a recombinant human TSH produced by mammalian cells, characterized in that said recombinant human TSH is submitted to a lentil fractionation, to give a lentil unbound fraction and a lentil bound fraction, the lentil unbound fraction being retained to yield a substantially unfucosylated glycoform of the recombinant TSH and the lentil bound fraction being retained to yield a glycoform which is substantially more fucosylated than said recombinant TSH.
31. A process according to claim 30, wherein:
- the recombinant human TSH is submitted to neuraminidase treatment, in particular a Clostridium perfringens or a Vibrio cholerae neuraminidase, prior to lentil fractionation, or
- the lentil bound fraction or the lentil unbound fraction of the recombinant human TSH is submitted to neuraminidase treatment, to yield a substantially unsialylated substantially unfucosylated glycoform of the recombinant human TSH or a glycoform of the recombinant human TSH which is substantially unsialylated and substantially more fucosylated than said recombinant human TSH.
32. A process according to any of claims 28 to 30, wherein
- the recombinant human TSH is submitted to sialylation to give an oversialylated glycoform of the recombinant human TSH, or both to neuraminidase treatment and to sialylation to give a resialylated glycoform of the recombinant human TSH, prior to lentil fractionation of said glycoform, or
- the lentil unbound fraction or the lentil bound fraction of the recombinant human TSH is submitted to sialylation, or sequentially to both neuraminidase treatment and sialylation, to yield a substantially unfucosylated oversialylated or resialylated glycoform of the recombinant human TSH or a glycoform of the recombinant human TSH which is oversialylated or resialylated and substantially more fucosylated than said recombinant human TSH.
33. A glycoform of recombinant human TSH such as obtainable according to any of claims 28 to 32.
34. A glycoform of a recombinant human TSH produced by mammalian cells which comprises from about 70% to about 100% α2,3 and o2,6 sialyl groups, in particular from about 70% to about 85 % Q2,3 sialyl groups and from about 15% to about 30% oQ,6 sialyl groups.
35. A glycoform of a recombinant human TSH produced by mammalian cells which comprises from about 70% to about 100 % oQ.,6 sialyl groups.
36. A glycoform of a recombinant human TSH produced by mammalian cells which comprises essentially no fucose.
37. A glycoform of a recombinant human TSH produced by mammalian cells which comprises from about 30% to about 100% fucose.
38. A glycoform of a recombinant human TSH produced by mammalian cells according to claim 36, which comprises essentially no fucose and no sialyl groups.
39. A glycoform of a recombinant human TSH produced by mammalian cells according to claim 37, which comprises essentially no sialyl groups and from about 30% to about 100% fucose.
40. A glycoform of a recombinant human TSH produced by mammalian cells according to claims 34 and 36, which comprises from about 70% to about 100% o2,3 sialyl and o2,6 sialyl groups, in particular from about 70% to about 85 % o2,3 sialyl groups and from about 15% to about 30% άZ,6 sialyl groups, and essentially no fucose.
41. A glycoform of a recombinant human TSH produced by mammalian cells according to claims 35 and 36, which comprises from about 70% to about 100 % oΩ.,6 sialyl groups and essentially no fucose.
42. A glycoform of a recombinant human TSH produced by mammalian cells according to claims 34 and 37, which comprises from about 70% to about 100% o2,3 sialyl and o2,6 sialyl groups, in particular from about 70% to about 85 % o2,3 sialyl groups and from about 15% to about 30% oΩ.,6 sialyl groups and from about 30% to about 100% fucose.
43. A glycoform of a recombinant human TSH produced by mammalian cells according to claims 35 and 37, which comprises from about 70% to about 100 % oQ.,6 sialyl groups and from about 30% to about 100% fucose
44. A kit for assaying specific glycoforms of a first glycoprotein, characterized in that it comprises at least one antibody such as screened according to the process of any of claims 2 to 26, said process comprising a step of determination of the binding between
- antibodies elicited against a first glycoprotein, and
- at least one glycoform of a second glycoprotein, said second glycoprotein being itself a glycoform of the first glycoprotein, wherein said glycoform of the second glycoprotein is selected from a group of glycoforms of the second glycoprotein, each glycoform of said group corresponding to a determined glycosylation state defined by a determined branching state and a determined fucosylation and / or sialylation state.
45. A kit according to claim 44, for assaying TSH in a biological sample, characterized in that it comprises:
- at least one capture-antibody selected from pools Ia, Ib, or III,
- at least a tracer-antibody selected from pools Ib, II, or III, provided that the capture-antibody and the tracer-antibody do not belong to the same pool, wherein:
- pool Ia is defined as being the pool of antibodies which can not bind to TSH once antibody BC27, S04 , Bl has already been bound to it,
- pool Ib is defined as being the pool of antibodies which can not bind to TSH once antibody B2,R1 orS06 has already been bound to it,
- pool II is defined as being the pool of antibodies which can not bind to TSH once antibody OCDl or R2 has already been bound to it,
- pool El is defined as being the pool of antibodies which can not bind to TSH once antibody B3 or S06 has already been bound to it.
46. A kit according to claim 44 or 45, characterized in that it comprises:
- a capture-antibody selected from pool Ia and a tracer antibody selected from pool Ib, or
- a capture-antibody selected from pool Ia and a tracer antibody selected from pool II, or
- a capture-antibody selected from pool Ib and a tracer antibody selected from pool π, or
- a capture-antibody selected from pool Ia and a tracer antibody selected from pool III, or - a capture-antibody selected from pool Ib and a tracer antibody selected from pool III, or
- a capture-antibody selected from pool III and a tracer antibody selected from pool H
47. A kit according to claim 45 or 46, characterized in that it further comprises a calibrant selected from the list comprising: pituitary human TSH, recombinant human TSH produced by mammalian cells, a glycoform of recombinant human TSH produced by mammalian cells which substantially less sialylated than said recombinant human TSH, a glycoform of recombinant human TSH produced by mammalian cells which is substantially more sialylated and/or less fucosylated than said recombinant human TSH, and a glycoform of recombinant human TSH according to any of claims 31 to 34.
48. The use of a glycoprotein selected from the list comprising: a glycoform of recombinant human TSH produced by mammalian cells which is substantially less sialylated than said recombinant human TSH, a glycoform of recombinant human TSH produced by mammalian cells which is substantially more sialylated and/or less fucosylated than said recombinant human TSH, and a glycoform of recombinant human TSH according to any of claims 33 to 43 for calibrating TSH immunoassays.
Priority Applications (6)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE602005022675T DE602005022675D1 (en) | 2004-02-04 | 2005-02-04 | METHOD FOR IDENTIFYING GLYCOPE-SPECIFIC ANTIBODIES |
| US10/588,220 US8431355B2 (en) | 2004-02-04 | 2005-02-04 | Process for screening glycoform-specific antibodies |
| CA2554968A CA2554968C (en) | 2004-02-04 | 2005-02-04 | Process for screening glycoform-specific antibodies |
| DK05701355.9T DK1711834T3 (en) | 2004-02-04 | 2005-02-04 | Method for screening glycoform-specific antibodies |
| EP05701355A EP1711834B1 (en) | 2004-02-04 | 2005-02-04 | Process for screening glycoform-specific antibodies |
| AT05701355T ATE476666T1 (en) | 2004-02-04 | 2005-02-04 | METHOD FOR IDENTIFYING GLYCOFORM-SPECIFIC ANTIBODIES |
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP04290290 | 2004-02-04 | ||
| EP04290290.8 | 2004-02-04 |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| WO2005076013A2 WO2005076013A2 (en) | 2005-08-18 |
| WO2005076013A3 WO2005076013A3 (en) | 2005-12-08 |
| WO2005076013B1 true WO2005076013B1 (en) | 2007-03-08 |
Family
ID=34833783
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PCT/EP2005/001160 WO2005076013A2 (en) | 2004-02-04 | 2005-02-04 | Process for screening glycoform-specific antibodies |
Country Status (8)
| Country | Link |
|---|---|
| US (1) | US8431355B2 (en) |
| EP (1) | EP1711834B1 (en) |
| AT (1) | ATE476666T1 (en) |
| CA (1) | CA2554968C (en) |
| DE (1) | DE602005022675D1 (en) |
| DK (1) | DK1711834T3 (en) |
| ES (1) | ES2350298T3 (en) |
| WO (1) | WO2005076013A2 (en) |
Families Citing this family (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP5727693B2 (en) * | 2005-12-23 | 2015-06-03 | ジェームス ディー． ケリー | Improved thyroid stimulating hormone receptor polypeptide agonist glycoform for treating metabolic syndrome |
| US20070218503A1 (en) * | 2006-02-13 | 2007-09-20 | Mitra Robi D | Methods of polypeptide identification, and compositions therefor |
| US7879799B2 (en) | 2006-08-10 | 2011-02-01 | Institute For Systems Biology | Methods for characterizing glycoproteins and generating antibodies for same |
| TWI488640B (en) | 2008-04-16 | 2015-06-21 | Ferring Int Ct Sa | Pharmaceutical preparation |
| TWI604850B (en) * | 2009-10-05 | 2017-11-11 | 菲瑞茵國際中心股份有限公司 | Pharmaceutical preparation |
| WO2012131306A1 (en) | 2011-03-31 | 2012-10-04 | Ferring B.V. | Pharmaceutical preparation |
| EP2900264A4 (en) * | 2012-09-26 | 2016-05-25 | Momenta Pharmaceuticals Inc | Glycoprotein preparations |
| CA2908407C (en) * | 2013-05-29 | 2022-06-14 | F. Hoffmann-La Roche Ag | Quantitative control of sialylation |
| JP6511045B2 (en) * | 2013-07-05 | 2019-05-08 | エフ．ホフマン−ラ ロシュ アーゲーＦ． Ｈｏｆｆｍａｎｎ−Ｌａ Ｒｏｃｈｅ Ａｋｔｉｅｎｇｅｓｅｌｌｓｃｈａｆｔ | Process for mono- and bi-sialylation of glycoproteins using N-terminally truncated beta-galactoside alpha-2,6-sialyltransferase variants |
| EP2824176A1 (en) * | 2013-07-11 | 2015-01-14 | Siamed'xpress | Methods for producing sialylated therapeutic proteins |
| EP3037527A1 (en) * | 2014-12-22 | 2016-06-29 | F. Hoffmann-La Roche AG | Sialyltransferase without CMP-dependent sialidase activity |
| CN107429237B (en) | 2014-12-22 | 2021-09-28 | 豪夫迈·罗氏有限公司 | CMP-dependent sialidase Activity |
| CN113960232B (en) * | 2021-10-28 | 2024-02-20 | 苏州大学 | Saliva-specific-fucosylation-based structural glycoprofile, and detection method and application thereof |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5976876A (en) * | 1995-12-11 | 1999-11-02 | The Trustees Of Columbia University In The City Of New York | Antibodies specific for hLH β core fragment |
| WO1999039202A1 (en) | 1998-02-03 | 1999-08-05 | The Trustees Of Columbia University In The City Of New York | DETERMINATION OF THE AMOUNT OF hLHβ CORE FRAGMENT IN A SAMPLE FROM A SUBJECT AND USES THEREOF |
| US6528269B1 (en) | 1998-06-22 | 2003-03-04 | Case Western Reserve University | Immunological agents specific for prion protein (PRP) |
| EP1143250A3 (en) | 2000-04-03 | 2004-11-17 | Inverness Medical Switzerland GmbH | Test methods and devices for analyte isoforms |
-
2005
- 2005-02-04 DE DE602005022675T patent/DE602005022675D1/en active Active
- 2005-02-04 US US10/588,220 patent/US8431355B2/en not_active Expired - Fee Related
- 2005-02-04 ES ES05701355T patent/ES2350298T3/en active Active
- 2005-02-04 DK DK05701355.9T patent/DK1711834T3/en active
- 2005-02-04 CA CA2554968A patent/CA2554968C/en not_active Expired - Fee Related
- 2005-02-04 WO PCT/EP2005/001160 patent/WO2005076013A2/en active Application Filing
- 2005-02-04 AT AT05701355T patent/ATE476666T1/en not_active IP Right Cessation
- 2005-02-04 EP EP05701355A patent/EP1711834B1/en not_active Not-in-force
Also Published As
| Publication number | Publication date |
|---|---|
| EP1711834A2 (en) | 2006-10-18 |
| DK1711834T3 (en) | 2010-11-29 |
| CA2554968C (en) | 2012-03-27 |
| US8431355B2 (en) | 2013-04-30 |
| CA2554968A1 (en) | 2005-08-18 |
| US20080199892A1 (en) | 2008-08-21 |
| WO2005076013A2 (en) | 2005-08-18 |
| DE602005022675D1 (en) | 2010-09-16 |
| ATE476666T1 (en) | 2010-08-15 |
| WO2005076013A3 (en) | 2005-12-08 |
| ES2350298T3 (en) | 2011-01-20 |
| EP1711834B1 (en) | 2010-08-04 |
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